Ontology highlight
ABSTRACT:
SUBMITTER: P Barros E
PROVIDER: S-EPMC5495472 | biostudies-literature | 2017 Mar
REPOSITORIES: biostudies-literature
P Barros Emília E Malmstrom Robert D RD Nourbakhsh Kimya K Del Rio Jason C JC Kornev Alexandr P AP Taylor Susan S SS Amaro Rommie E RE
Biochemistry 20170306 10
Close-range electrostatic interactions that form salt bridges are key components of protein stability. Here we investigate the role of these charged interactions in modulating the allosteric activation of protein kinase A (PKA) via computational and experimental mutational studies of a conserved basic patch located in the regulatory subunit's B/C helix. Molecular dynamics simulations evidenced the presence of an extended network of fluctuating salt bridges spanning the helix and connecting the t ...[more]